Reviewed, UniProtKB/Swiss-Prot A9HYU0 (GLMM_BORPD)

Names and origin

Protein names

Recommended name:
    Phosphoglucosamine mutase
    EC=5.4.2.10

Gene names

Name:	glmM
Ordered Locus Names:	Bpet3529

Organism

Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448) [Complete proteome] [HAMAP]

Taxonomic identifier

340100 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Alcaligenaceae › Bordetella

Protein attributes

Sequence length	447 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the conversion of glucosamine-6-phosphate to glucosamine-1-phosphate By similarity.
Catalytic activity	Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate. HAMAP MF_01554
Cofactor	Binds 1 magnesium ion per subunit By similarity.
Post-translational modification	Activated by phosphorylation By similarity.
Sequence similarities	Belongs to the phosphohexose mutase family.

Ontologies

Keywords
Ligand	Magnesium Metal-binding
Molecular function	Isomerase
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	magnesium ion binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoglucosamine mutase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 447	447	Phosphoglucosamine mutase HAMAP MF_01554		PRO_1000201065
Sites
	Active site	108	1	Phosphoserine intermediate By similarity
	Metal binding	108	1	Magnesium; via phosphate group By similarity
	Metal binding	247	1	Magnesium By similarity
	Metal binding	249	1	Magnesium By similarity
	Metal binding	251	1	Magnesium By similarity
Amino acid modifications
	Modified residue	108	1	Phosphoserine By similarity

Sequences

	Sequence		Length	Mass (Da)
	A9HYU0-1 [UniParc]. Last modified February 5, 2008. Version 1. Checksum: 8ACF2AFC05FAE70D	FASTA	447	47,521
	10 20 30 40 50 60 MTQRKYFGTD GVRGEVGGEV INAAFALRLG YAAGRVLARQ HGGRGGSRPQ VVIGKDTRIS 70 80 90 100 110 120 GYMLESALEA GLSAAGIDVL LAGPVPTPAV AYLTRALRLV AGIVISASHN PYQDNGIKFF 130 140 150 160 170 180 SAQGMKLPDE VEAEIEAALH EPLGCVGSEA LGRARRMQDS QGRYIEFCKS TFPNDLDLNG 190 200 210 220 230 240 VKIVVDAAHG AAYNVAPHVF RELGADVHAI GVSPDGFNIN EGVGALHPES LARAVRERGA 250 260 270 280 290 300 HLGIALDGDA DRLQMVDGDG RIYNGDELLY AIVRERMSRG TVAGVVGTLM TNYGFELEMQ 310 320 330 340 350 360 RLGVGFERAK VGDRYVMEQM QARGWLYGGE SSGHLICLDC HTTGDGIIAA LQVLTALRRG 370 380 390 400 410 420 NVPLADWLGD LRMYPQKMIN VPLAPGTDWK SHAGLAAATR AVEAELAGRG RVLIRASGTE 430 440 PKLRLMVEAE EPALAASCAE KLAASLA

References

[1]

"The missing link: Bordetella petrii is endowed with both the metabolic versatility of environmental bacteria and virulence traits of pathogenic Bordetellae." Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H., Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V., Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S., Linke B., Meyer F. , Mormann S., Nakunst D., Rueckert C., Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T., Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O., Martinez-Arias R. BMC Genomics 9:449-449(2008) [PubMed: 18826580] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	AM902716 Genomic DNA. Translation: CAP43872.1.
RefSeq	YP_001632140.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	5819723.
GenomeReviews	Gene locus Bpet3529 in contig AM902716_GR.
KEGG	bpt:Bpet3529.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	STHPEAM.
Family and domain databases
HAMAP	MF_01554. [Tree]
InterPro	IPR005844. A-D-PHexomutase_a/b/a-I. IPR016055. A-D-PHexomutase_a/b/a-I/II/III. IPR005845. A-D-PHexomutase_a/b/a-II. IPR005846. A-D-PHexomutase_a/b/a-III. IPR005843. A-D-PHexomutase_C. IPR016066. A-D-PHexomutase_CS. IPR005841. A-D-PHexomutase_N. IPR006352. GlmM. [Graphical view]
Gene3D	G3DSA:3.40.120.10. A-D-PHexomutase_a/b/a-I/II/III. 3 hits.
Pfam	PF02878. PGM_PMM_I. 1 hit. PF02879. PGM_PMM_II. 1 hit. PF02880. PGM_PMM_III. 1 hit. PF00408. PGM_PMM_IV. 1 hit. [Graphical view]
PRINTS	PR00509. PGMPMM.
TIGRFAMs	TIGR01455. glmM. 1 hit.
PROSITE	PS00710. PGM_PMM. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

GLMM_BORPD

Accession

Primary (citable) accession number: A9HYU0

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 14, 2009
Last sequence update:	February 5, 2008
Last modified:	November 3, 2009
This is version 22 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)